{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,12]],"date-time":"2026-02-12T14:02:55Z","timestamp":1770904975061,"version":"3.50.1"},"reference-count":53,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2019,3,23]],"date-time":"2019-03-23T00:00:00Z","timestamp":1553299200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100004281","name":"Narodowe Centrum Nauki","doi-asserted-by":"publisher","award":["2015\/17\/B\/NZ1\/00873"],"award-info":[{"award-number":["2015\/17\/B\/NZ1\/00873"]}],"id":[{"id":"10.13039\/501100004281","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2019,6]]},"abstract":"<jats:p>Outer surface protein C (OspC) is one of the most abundant surface lipoproteins produced during early infection by the <jats:italic>Borrelia<\/jats:italic> spirochete, the causative agent of Lyme disease. The high sequence variability of the <jats:italic>ospC<\/jats:italic> gene results in the production of several and strongly divergent OspC types. One of the known roles of OspC is the recruitment of blood components, including complement regulators, to facilitate the bloodstream survival of <jats:italic>Borrelia<\/jats:italic> at an essential stage of host infection. Here, we identify and describe a new interaction between OspC and human fibrinogen. To test the ability of OspC to bind fibrinogen, we developed a microscale thermophoresis assay using four fluorescently labeled types of OspC. We show that OspC binds fibrinogen tightly, with nanomolar <jats:italic>K<\/jats:italic><jats:sub>d<\/jats:sub>, and that the binding depends on the OspC type. The binding assays combined with <jats:styled-content style=\"fixed-case\">SAXS<\/jats:styled-content> studies allowed us to map the OspC\u2010binding site on the fibrinogen molecule. Spectrometric measurements of fibrinogen clotting in the presence of OspC indicate that OspC negatively influences the clot formation process. Taken together, our findings are consistent with the hypothesis that OspC interacts with blood protein partners to facilitate <jats:italic>Borrelia<\/jats:italic> spreading by the hematogenous route.<\/jats:p>","DOI":"10.1111\/febs.14810","type":"journal-article","created":{"date-parts":[[2019,3,15]],"date-time":"2019-03-15T07:37:37Z","timestamp":1552635457000},"page":"2415-2428","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["<i>Borrelia<\/i> outer surface protein C is capable of human fibrinogen binding"],"prefix":"10.1111","volume":"286","author":[{"given":"Paulina","family":"Bierwagen","sequence":"first","affiliation":[{"name":"Institute of Bioorganic Chemistry Polish Academy of Sciences Poznan Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kamil","family":"Szpotkowski","sequence":"additional","affiliation":[{"name":"Institute of Bioorganic Chemistry Polish Academy of Sciences Poznan Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mariusz","family":"Jaskolski","sequence":"additional","affiliation":[{"name":"Institute of Bioorganic Chemistry Polish Academy of Sciences Poznan Poland"},{"name":"Department of Crystallography Faculty of Chemistry A. 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